ID   ACL2_SCHPO              Reviewed;         492 AA.
AC   O13907;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Probable ATP-citrate synthase subunit 2;
DE            EC=2.3.3.8;
DE   AltName: Full=ATP-citrate (pro-S-)-lyase 2;
DE   AltName: Full=Citrate cleavage enzyme subunit 2;
GN   ORFNames=SPAC22A12.16;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: ATP citrate-lyase is the primary enzyme responsible for the
CC       synthesis of cytosolic acetyl-CoA. Has a central role in de novo lipid
CC       synthesis (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ADP + oxaloacetate + phosphate = ATP + citrate +
CC         CoA; Xref=Rhea:RHEA:21160, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:456216; EC=2.3.3.8;
CC   -!- SUBUNIT: Composed of two subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the succinate/malate
CC       CoA ligase beta subunit family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the succinate/malate
CC       CoA ligase alpha subunit family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB16586.1; -; Genomic_DNA.
DR   PIR; T38156; T38156.
DR   RefSeq; NP_593246.1; NM_001018643.2.
DR   AlphaFoldDB; O13907; -.
DR   SMR; O13907; -.
DR   BioGRID; 278302; 9.
DR   STRING; 4896.SPAC22A12.16.1; -.
DR   iPTMnet; O13907; -.
DR   MaxQB; O13907; -.
DR   PaxDb; O13907; -.
DR   PRIDE; O13907; -.
DR   EnsemblFungi; SPAC22A12.16.1; SPAC22A12.16.1:pep; SPAC22A12.16.
DR   GeneID; 2541811; -.
DR   KEGG; spo:SPAC22A12.16; -.
DR   PomBase; SPAC22A12.16; -.
DR   VEuPathDB; FungiDB:SPAC22A12.16; -.
DR   eggNOG; KOG1254; Eukaryota.
DR   HOGENOM; CLU_006587_3_1_1; -.
DR   InParanoid; O13907; -.
DR   OMA; ANGRVWT; -.
DR   PhylomeDB; O13907; -.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   Reactome; R-SPO-75105; Fatty acyl-CoA biosynthesis.
DR   PRO; PR:O13907; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003878; F:ATP citrate synthase activity; ISS:PomBase.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; ISS:PomBase.
DR   GO; GO:0006101; P:citrate metabolic process; IC:PomBase.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; ISS:PomBase.
DR   Gene3D; 3.40.50.261; -; 1.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR032263; Citrate-bd.
DR   InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF16114; Citrate_bind; 1.
DR   SUPFAM; SSF52210; SSF52210; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; ATP-binding; Cytoplasm; Lipid biosynthesis;
KW   Lipid metabolism; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..492
FT                   /note="Probable ATP-citrate synthase subunit 2"
FT                   /id="PRO_0000340113"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   492 AA;  53943 MW;  7B3FE2529B786CDA CRC64;
     MSAKSIREYD GKAVLAYWLN RSPSISKEEY KTVSATPAVQ LAQIQFPLPT LVIPAESTTY
     REVVEDVFAK VEQEHPWVKE TKLVAKPDQL IKRRGKSGLL KLNATWDEAK EWIRERAGKN
     QKVQHAVGYL TTFLVEPFVP HPPNTEYYIN INSVREGDWI LFCNEGGVDV GDVDAKARKL
     LVPVRLSEFP SRATIASTLL SDIPVEQHES LVDFIIRLYS VYVDCQFTYL EINPLVVIPT
     AKGADVFYLD LAAKLDQTAE FECGAKWAVA RAPESLGIKT SGEESGAINA DHGPPMVFPA
     PFGRELSKEE AYVQGLDAKT GASLKLTILN AEGRVWNLVA GGGASVVYAD AVAVNGAADE
     LANYGEYSGA PTDGQTYEYA KTVLDLMTRG EPRADGKVLF IGGGIANFTS PAVTFRAIAR
     ALGDYKDKLH AHKVSIWVRR AGPNYQEGLR VIREAGKKFD LPLKVYGPEC HISGIVPMGL
     GKAPVEAEWQ MA